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TCL1B protein, human

TCL1B (T-Cell Leukemia/Lymphoma 1B) is a protein-coding gene that plays a crucial role in the development and progression of certain types of cancer, particularly T-cell leukemia and lymphoma.
This gene is a member of the TCL1 gene family and acts as an oncogene, contributing to the uncontrolled proliferation of T-cells.
Understanding the functions and regulation of TCL1B is essential for developing effective targeted therapies and improving patient outcomes.
Researchers can leverage the power of PubCompare.ai to optimize their TCL1B protein research, enhanceing reproducibility and accuracy by identifying the most reliable and effective experimental protocols from literature, pre-prints, and patents.
Experiance the future of protein research today with this AI-powered platform.

Most cited protocols related to «TCL1B protein, human»

Sparse Labeling of Cortical Neurons for Imaging

Cited 183 times

Constructs used to produce AAV included pGP-AAV-syn-GCaMP-WPRE and the Cre recombinase-activated construct pGP-AAV-syn-flex-GCaMP-WPRE. Virus was injected slowly (30 nL in 5 minutes) at a depth of 250 μm into the primary visual cortex (two sites, 2.5 and 2.9 mm lateral from the lambda suture). For population imaging and electrophysiology (Fig 2-3), AAV2/1-syn-GCaMP-WPRE virus (titer: ∼10^{11 (link)} -10^{12 (link)} genomes/mL) was injected into the visual cortex of C57BL/6J mice (1.5-2 months old)^{6 (link)}. For dendritic imaging (Fig 4, 5 and 6a-f), sparse labeling was achieved by injecting a mixture of diluted AAV2/1-syn-Cre particles (titer: ∼10^{12 (link)} genomes/mL, diluted 8000-20,000 fold in PBS) and high titer, Cre-dependent GCaMP6s virus (∼8×10^{11 (link)} genomes/mL). This produces strong GCaMP6 expression in a small subset of neurons (∼3-5 cells in a 250 μm × 250 μm × 250 μm volume), defined by Cre expression^{56 (link)}. Both pyramidal (Fig. 4-5) and GABAergic (Fig. 6) neurons were labeled using this approach, but they could be distinguished based on the presence or absence of dendritic spines. Post hoc immunolabeling further identified the imaged cells. For specific labeling of parvalbumin interneurons (Fig. 6g and Supplementary Fig. 12), Cre-dependent GCaMP6s AAV was injected into the visual cortex of PV-IRES-Cre mice^{57 (link)}. Individual somata (Supplementary Fig. 12) and dendritic segments could be recognized (Fig. 6 g, h, total length of imaged dendrite: 2.86 mm), but the high labeling density made it difficult to track individual dendrites over long distances.

Chen T.W., Wardill T.J., Sun Y., Pulver S.R., Renninger S.L., Baohan A., Schreiter E.R., Kerr R.A., Orger M.B., Jayaraman V., Looger L.L., Svoboda K, & Kim D.S. (2013). Ultra-sensitive fluorescent proteins for imaging neuronal activity. Nature, 499(7458), 295-300.

Publication 2013

Cells Cre recombinase Dendrites Dendritic Spines Genome Internal Ribosome Entry Sites Interneurons Mice, Inbred C57BL Neurons Parvalbumins Striate Cortex Sutures TCL1B protein, human Virus Visual Cortex

AAV Injection into Mouse Visual Cortex

Cited 19 times

Constructs used to produce AAV included pGP-AAV-SYN1-red GECI-WPRE and the cre-recombinase-activated construct pGP-AAV-FLEX-SYN1-red GECI-WPRE. Virus (titer: ~0.7-3x10¹³ genomes/ml, R-CaMP2 promoter was CaMKII) was slowly injected (25–30 nl over 5 min) through a thinned skull into the primary visual cortex (1–2 injection sites at variable depths; 2.7 mm lateral and 0.2 mm anterior to lambda suture; 250 μm deep for L2/3 imaging, 250 μm and 450 μm for L4 imaging, 500 μm for L5 imaging, and 650 μm and 900 μm for L6 imaging).

Dana H., Mohar B., Sun Y., Narayan S., Gordus A., Hasseman J.P., Tsegaye G., Holt G.T., Hu A., Walpita D., Patel R., Macklin J.J., Bargmann C.I., Ahrens M.B., Schreiter E.R., Jayaraman V., Looger L.L., Svoboda K, & Kim D.S. (2016). Sensitive red protein calcium indicators for imaging neural activity. eLife, 5, e12727.

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Publication 2016

Calmodulin-Dependent Protein Kinase II Cranium Cre recombinase Genome Striate Cortex Sutures TCL1B protein, human Vascular Access Ports Virus

Preparation and Characterization of α-Synuclein Fibrils

Cited 11 times

Brainstem and spinal cord of aged symptomatic M83 mice were dissected from brains previously stored at −80°C. Tissue was sonicated in sterile PBS (100 mg per 1 ml of buffer) with a handheld probe (QSonica). Homogenates were cleared by centrifugation for 5 min (3,000 g, 4°C) and the resultant supernatant (lysate) was recovered and stored at −80°C until injection. Purification of recombinant α-Syn proteins and in vitro fibril assembly was performed as previously described (Murray et al., 2003 (link); Luk et al., 2009 (link)) using human α-Syn^1-120Myc or WT full-length human α-Syn (5 mg/ml). PFFs were collected after 5 d of incubation at 37°C. PFF preparations were diluted into sterile PBS and sonicated briefly before intracerebral injection.

Luk K.C., Kehm V.M., Zhang B., O’Brien P., Trojanowski J.Q, & Lee V.M. (2012). Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. The Journal of Experimental Medicine, 209(5), 975-986.

Publication 2012

Brain Brain Stem Buffers Centrifugation Homo sapiens Mice, Laboratory Recombinant Proteins Spinal Cord Sterility, Reproductive TCL1B protein, human Tissues

Characterization of α-Synuclein Antibodies

Cited 10 times

Ser(P)-129 α-syn antibodies and the antibody raised to total alpha synuclein were commercially available and purchased from Abcam (EP1536Y,81a, MJF-R13), Wako USA (pSyn#64), and BD Bioscience (Syn1). Vendors report that the Ser(P)-129 α-syn monoclonal antibodies were raised against synthetic human α-synuclein peptide spanning 124–134 region with a phosphorylated Ser 129 residue. This peptide sequence was originally constructed by Fujiwara et al, and used in their seminal work that led to the discovery of extensive α-syn phosphorylation at Ser 129 reside in Lewy bodies (Fujiwara et al., 2002 (link)). Monoclonal antibodies developed against synthetic α-syn aa 124–134 (phospho 129) peptide were validated using other antibodies that label Lewy bodies in post-mortem brain sections (Baba et al., 1998 (link); Fujiwara et al., 2002 (link)).
Clone EP1536Y is a monoclonal IgG antibody raised in rabbit and may be suitable for use in immunoblotting and immunohistochemistry (Perez-Revuelta et al., 2014 (link); Prusiner et al., 2015 (link); Tuttle et al., 2016 (link); Arawaka et al., 2017 (link)). Clone 81a is mouse IgG2a also used in immunoblot and immunohistochemistry applications (Tuttle et al., 2016 (link); Dieriks et al., 2017 (link)). MJF-R13 is a rabbit IgG monoclonal antibody used in immunoblotting experiments (Brahmachari et al., 2016 (link)). Clone pSyn#64 is mouse IgG1 suitable for immunoblotting and immunohistochemistry (Jiang et al., 2016 (link)). Clone Syn1 is mouse IgG1 raised to rat α-syn peptide aa 15–123, has not been further mapped within that peptide, but has been previously evaluated for specificity (Perrin et al., 2003 (link)). For additional primary antibody information and secondary antibody information see Table 1. Optimal secondary concentration was determined by serial dilution starting with the vendor recommendations. pS129-α-syn antibody concentration was confirmed using a BCA Protein Assay Kit (Pierce) with a γ-globulin protein standard, and all antibodies diluted to working stock concentrations of 0.1 mg mL⁻¹.

Delic V., Chandra S., Abdelmotilib H., Maltbie T., Wang S., Kem D., Scott H.J., Underwood R.N., Liu Z., Volpicelli-Daley L.A, & West A.B. (2018). Sensitivity and Specificity of Phospho-Ser129 α-Synuclein Monoclonal Antibodies. The Journal of comparative neurology, 526(12), 1978-1990.

Publication 2018

alpha-Synuclein Antibodies Autopsy Biological Assay Brain Clone Cells gamma-Globulin Homo sapiens IgG1 IgG2A Immunoglobulin G Immunoglobulins Immunohistochemistry Lewy Bodies Mice, House Monoclonal Antibodies Peptides Phosphorylation Proteins Rabbits TCL1B protein, human Technique, Dilution

Preparation of α-Synuclein Fibrils for Cellular Studies

Cited 10 times

For cellular experiments, α-syn proteins were assembled into filaments by incubation at 37°C at concentrations greater than 5 mg/ml in sterile phosphate buffered saline (PBS, Invitrogen) with continuous shaking at 1050 rpm (Thermomixer R, Eppendorf, Westbury, NY). Experimentation was planned so that α-syn would be visibly assembled (by filamentous clusters observed in the solution) by the day of cellular experimentation. α-Syn fibrils were diluted to a concentration of 1 mg/ml in sterile PBS and treated by water bath sonication for a minimum of 2 hours. In experiments where large fibrils were separated from small polymers, diluted fibrillized α-syn (prior to sonication) was centrifuged at 16,000 × g for 5 min, and the supernatant was removed and the pellet was re-suspended in sterile PBS. Protein concentrations of the original diluted fibrils and the supernatant were measured by BCA protein assay (Pierce). Concentration of the large fibrils was determined as the concentrations of [total - supernatant]. All samples were sonicated in a water bath prior to addition to cell culture media. Unless otherwise specified, cells were treated with 1 μM of recombinant 21–140 α-syn fibril mix.

Waxman E.A, & Giasson B.I. (2010). A Novel, High-Efficiency Cellular Model of Fibrillar α-Synuclein Inclusions and the Examination of Mutations that Inhibit Amyloid Formation. Journal of neurochemistry, 113(2), 374-388.

Publication 2010

Bath Biological Assay Cell Culture Techniques Cells Culture Media Cytoskeletal Filaments Phosphates Polymers Proteins Saline Solution Sterility, Reproductive TCL1B protein, human

Most recents protocols related to «TCL1B protein, human»

Measuring PAL Activity and Phenylpyruvate

Not available on PMC !

Example 64

A 1:100 back-dilution from overnight culture of SYN-PKU-2002 was grown to early log phase for 1.5 h before moving to the anaerobic chamber for 4 hours in the presence of 1 mM IPTG and 0.1% arabinose for induction as described herein. To perform activity assay, 1e8 cells were resuspended and incubated in assay buffer (M9 media with 0.5% glucose, 50 mM Phe, and 50 mM MOPS with 50 mM phenylalanine). Supernatant samples were taken over time and TCA (the product of PAL) was measured by absorbance at 290 nm to determine the rate of TCA production/PAL activity. Phenylpyruvate was measured using LCMS methods described herein. Results are shown in FIG. 16A and FIG. 16B.

US11879123B2. Bacteria for the treatment of disorders (2024-01-23). Synlogic Operating Company, Inc. [US]. Inventors: Dean Falb [US], Adam B. Fisher [US], Vincent M. Isabella [US], Jonathan W. Kotula [US], David Lubkowicz [US], Paul F. Miller [US], Yves Millet [US], Sarah Elizabeth Rowe [US].

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Patent 2024

3-phenylpyruvate Arabinose Biological Assay Buffers Cells Glucose Isopropyl Thiogalactoside Laser Capture Microdissection morpholinopropane sulfonic acid Phenylalanine TCL1B protein, human Technique, Dilution

Evaluating Ceftriaxone Degradation by SYN-004

Not available on PMC !

Example 8

Ceftriaxone (at 3 ug/ml or 1500 ug/ml) was mixed with human intestinal chyme alone, or with chyme plus SYN-004 (8 ug/ml) or with chyme plus the beta-lactamase inhibitor sulbactam, (20 mg/ml) or chyme plus both and then the samples were flash frozen. The flash frozen samples were thawed on ice and sulbactam was added to some samples, the protein was precipitated with acetonitrile and the samples were analyzed for ceftriaxone concentration by LC/MS-MS. The table below provides results from triplicate samples.

Percent of untreated control sample

Sample3 ug/ml ceftriaxone1500 ug/ml ceftriaxone

Ceftriaxone alone100% ¹100% ¹

Ceftriaxone plus SYN-004 0% 0%

Ceftriaxone plus SYN-004, sulbactam added at 0% 2%

sample thaw

Ceftriaxone plus sulbactam and then add SYN-004ND ²53.5%

¹Nominally set at 100%

²Not done

Even at 20 mg/ml Sulbactam, 8 ug/ml of SYN-004 could not be inhibited (that's a molar ratio of about 287,000:1, sulbactam to SYN-004). Altogether, these data suggested that Sulbactam did not substantially inhibit SYN-004 activity in intestinal chyme.

US11872268B2. Safe and effective beta-lactamase dosing for microbiome protection (2024-01-16). Theriva Biologics, Inc. [US]. Inventors: Joseph Sliman [US].

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Patent 2024

acetonitrile beta-Lactamase Inhibitors Cardiac Arrest Ceftriaxone Defecation Freezing Homo sapiens Intestines Molar Proteins Sulbactam SYN-004 Tandem Mass Spectrometry TCL1B protein, human

Comprehensive Neuronal Marker Staining

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2023

alexa fluor 488 Alexa Fluor 555 Hybridomas Neural Cell Adhesion Molecules SOX10 Transcription Factor TCL1B protein, human TUBB3 protein, human

Immunofluorescence Staining of Mouse Brain Sections

For immunofluorescence, mice were PBS and 4% PFA-perfused, brains were harvested, post-fixed in PFA, dehydrated in 30% sucrose and embedded in OCT. 14 μm-thick frozen sections were permeabilized and blocked in 0.5% TritonX-100 and 5% Bovine Serum Albumin in 0.5% TritonX-100/1X PBS, respectively. Sections were incubated with primary antibodies in blocking solution overnight at 4 °C followed by incubation with 488, 564 and 647 Alexa-Fluor conjugated secondary antibodies for 1 h at room temperature. After secondary antibody incubations, sections were washed with 0.1% NP-40/1X PBS. DAPI was used to detect cells nuclei. Sections were mounted using ProLong™ Diamond Antifade Mountant (P36961; Life Technologies). The primary antibodies used were: Tyrosine Hydroxylase (TH) (1:1000; ab113, Abcam), hα-SYN (1:300; ab138501, Abcam), TMEM119 (1:500; ab209064, Abcam), CD16/32 (1:100; #101301, BioLegend) and CD3 (1:200; 100347, BioLegend). For staining involving hα-SYN, heat-mediated antigen retrieval was performed using DAKO retrieval solution (S1700; DAKO). All images were acquired with a Nikon Ti-E Eclipse Microscope using a 20× objective (Plan-Apo, 0.75 numerical aperture) or a 60× oil objective (Plan-Apo, 1.4 numerical aperture). Confocal images were acquired using CREST X-Light V2 Spinning Disk. Z-stacks of 60× images were collected at 0.5 μm increments with a total thickness of ~ 6 μm. Images were captured with an ORCA-fusion camera (C14440-20UP, Hamamatsu) or an Andor Zyla camera (Zyla 4.2 sCMOS, Oxford Instruments). Large scan function with Z step focus was used to capture stitched images of the SN using a 20× objective. Confocal images are shown as maximum intensity projection images. Images are representative of the respective staining and were processed and analyzed using NIS-elements advanced research software (Nikon Instrument Inc) and FIJI-Image J open software.

Torrente D., Su E.J., Schielke G.P., Warnock M., Mann K, & Lawrence D.A. (2023). Opposing effects of β-2 and β-1 adrenergic receptor signaling on neuroinflammation and dopaminergic neuron survival in α-synuclein-mediated neurotoxicity. Journal of Neuroinflammation, 20, 56.

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Publication 2023

Antibodies Antigens Brain Cell Nucleus Crista Ampullaris DAPI Diamond Fluorescent Antibody Technique Frozen Sections Immunoglobulins Light Microscopy Mus Nonidet P-40 Orcinus orca Radionuclide Imaging Serum Albumin, Bovine Sucrose TCL1B protein, human Tyrosine 3-Monooxygenase

Scoping Neuronal Diversity in Mouse Hypothalamus

Cell Ranger h5 files were read into Seurat v4 ^{98 (link)} in R (version 4.1.0) and RStudio (version 1.4.1717) and merged by brain region (DMH, SCN) for clustering analysis. We filtered the initial datasets to remove low quality samples (i.e., cells with less than 100 genes detected or greater than 0.5% mitochondrial reads). We then log-normalized the data; selected 2,000 most variable genes (“feature selection”), and scaled gene expression. We performed Principal Component Analysis (PCA) to linearly reduce the dimensionality of the highly variable gene set. We defined distance metrics based on K-nearest neighbor analysis, grouped cells with Louvian algorithm modality optimization, and visualized cell embeddings in low-dimensional space with Uniform Manifold Approximation and Projection (UMAP) nonlinear dimensionality reduction. To focus our analysis on neurons, we subsetted neuronal clusters based on their enriched expression of neuronal marker genes (Syt1, Syn1, Tubb3). To correct for batch effects, we integrated across sample batches using Seurat’s function for reciprocal principal component analysis (RPCA). Next, we subsetted region-specific clusters based on expression of positive and negative marker genes for each target brain region (SCN, DMH), as described in the next section. We reclustered the identified DMH and SCN neurons using the following parameters: DMH, 2,000 most variable genes, first 15 PCs, resolution setting of 0.8; SCN, 2,000 most variable genes, first 13 PCs, resolution setting of 0.5 Finally, we assessed cluster markers with the Wilcoxon Rank Sum test using Seurat default settings. Cluster markers were selected based on top p-values (adjusted to correct for multiple comparisons), high percent expression within the cluster and low percent expression outside of the cluster, and validated based on Allen Brain Atlas mouse in situ hybridization data and previous literature.

Tang Q., Godschall E., Brennan C.D., Zhang Q., Abraham-Fan R.J., Williams S.P., Güngül T.B., Onoharigho R., Buyukaksakal A., Salinas R., Olivieri J.J., Deppmann C.D., Campbell J.N., Podyma B, & Güler A.D. (2023). A leptin-responsive hypothalamic circuit inputs to the circadian feeding network. bioRxiv.

Publication Preprint 2023

Brain Cells Gene Expression Genes Genetic Markers In Situ Hybridization Mice, Laboratory Mitochondrial Inheritance Neurons Suprachiasmatic Nucleus Neurons SYT1 protein, human TCL1B protein, human TUBB3 protein, human

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What is the TCL1B protein and what is its role in human health?

The TCL1B (T-Cell Leukemia/Lymphoma 1B) protein is a crucial player in the development and progression of certain types of cancer, particularly T-cell leukemia and lymphoma. As a member of the TCL1 gene family, TCL1B acts as an oncogene, contributing to the uncontrolled proliferation of T-cells. Understanding the functions and regulation of this protein is essential for developing effective targeted therapies and improving patient outcomes.

How can PubCompare.ai help with TCL1B protein research?

PubCompare.ai is an AI-powered platform that can assist researchers in optimizing their TCL1B protein research. The platform allows you to screen protocol liteature more eficiently, leveraging AI to pinpoint critical insights. PubCompare.ai can help researchers identify the most effective protocols related to TCL1B protein, human for their specific research goals. The platform's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy.

What are some common challenges in working with the TCL1B protein, human?

One of the key challenges in working with the TCL1B protein, human is ensuring the reliability and reproducibility of experimental protocols. Researchers may encounter variations in experimental methods and conditions, which can impact the effectiveness and accuracy of their findings. PubCompare.ai can help address this by allowing researchers to identify the most reliable and effective protocols from the literature, pre-prints, and patents, ensuring that their TCL1B protein experiments are optimized for success.

Are there different variations or types of the TCL1B protein that researchers should be aware of?

The TCL1B protein is a member of the TCL1 gene family, which includes several related proteins. While the core functions of TCL1B are well-understood, researchers should be aware that there may be subtle variations or isoforms of the protein that could have unique properties or roles in different cellular contexts. Understanding these nuances can be crucial for developing targeted therapies or designing experiments that accurately capture the complexities of TCL1B biology.

More about "TCL1B protein, human"

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